Zinc in PDB 6rbc: X-Ray Structure of Human Glutamate Carboxypeptidase II (Gcpii) in Complex with A Inhibitor KB1157

All present enzymatic activity of X-Ray Structure of Human Glutamate Carboxypeptidase II (Gcpii) in Complex with A Inhibitor KB1157:
3.4.17.21;

The structure of X-Ray Structure of Human Glutamate Carboxypeptidase II (Gcpii) in Complex with A Inhibitor KB1157, PDB code: 6rbc was solved by C.Barinka, Z.Kutil, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	45.00 / 1.77
Space group	I 2 2 2
Cell size a, b, c (Å), α, β, γ (°)	101.551, 130.470, 159.045, 90.00, 90.00, 90.00
R / Rfree (%)	16.4 / 19.1

The structure of X-Ray Structure of Human Glutamate Carboxypeptidase II (Gcpii) in Complex with A Inhibitor KB1157 also contains other interesting chemical elements:

Iodine	(I)	1 atom
Calcium	(Ca)	1 atom
Chlorine	(Cl)	1 atom

The binding sites of Zinc atom in the X-Ray Structure of Human Glutamate Carboxypeptidase II (Gcpii) in Complex with A Inhibitor KB1157 (pdb code 6rbc). This binding sites where shown within 5.0 Angstroms radius around Zinc atom.
In total 2 binding sites of Zinc where determined in the X-Ray Structure of Human Glutamate Carboxypeptidase II (Gcpii) in Complex with A Inhibitor KB1157, PDB code: 6rbc:
Jump to Zinc binding site number: 1; 2;

Zinc binding site 1 out of 2 in the X-Ray Structure of Human Glutamate Carboxypeptidase II (Gcpii) in Complex with A Inhibitor KB1157


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of X-Ray Structure of Human Glutamate Carboxypeptidase II (Gcpii) in Complex with A Inhibitor KB1157 within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn813 b:25.1 occ:1.00 NE2 A:HIS553 2.0 24.7 1.0 OD2 A:ASP387 2.0 25.8 1.0 O A:HOH1247 2.1 23.0 1.0 OE2 A:GLU425 2.1 23.8 1.0 O3 A:JX5817 2.3 27.8 1.0 OE1 A:GLU425 2.4 24.3 1.0 CD A:GLU425 2.6 24.0 1.0 CE1 A:HIS553 2.9 25.2 1.0 CG A:ASP387 3.0 26.7 1.0 C8 A:JX5817 3.1 27.9 1.0 CD2 A:HIS553 3.1 24.8 1.0 ZN A:ZN814 3.3 24.6 1.0 OD1 A:ASP387 3.4 22.5 1.0 N4 A:JX5817 3.8 24.0 1.0 N3 A:JX5817 3.9 24.8 1.0 C9 A:JX5817 4.0 23.9 1.0 C7 A:JX5817 4.0 25.5 1.0 ND1 A:HIS553 4.1 24.2 1.0 CE1 A:TYR552 4.1 24.2 1.0 CG A:GLU425 4.1 22.5 1.0 OE1 A:GLU424 4.1 23.3 1.0 O A:HOH1066 4.1 25.3 1.0 CG A:HIS553 4.2 25.0 1.0 OH A:TYR552 4.3 25.7 1.0 CB A:ASP387 4.3 25.9 1.0 NE2 A:HIS377 4.5 22.9 1.0 C13 A:JX5817 4.6 26.1 1.0 CD1 A:TRP381 4.6 28.0 1.0 CZ A:TYR552 4.6 26.1 1.0 NE1 A:TRP381 4.7 26.1 1.0 CE1 A:HIS377 4.7 24.2 1.0 O7 A:JX5817 4.8 26.0 1.0 OD2 A:ASP453 4.9 25.6 1.0 CD A:GLU424 5.0 23.5 1.0

Zinc binding site 2 out of 2 in the X-Ray Structure of Human Glutamate Carboxypeptidase II (Gcpii) in Complex with A Inhibitor KB1157


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 2 of X-Ray Structure of Human Glutamate Carboxypeptidase II (Gcpii) in Complex with A Inhibitor KB1157 within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn814 b:24.6 occ:1.00 O A:HOH1247 1.7 23.0 1.0 NE2 A:HIS377 2.0 22.9 1.0 OD2 A:ASP453 2.0 25.6 1.0 OD1 A:ASP387 2.0 22.5 1.0 CG A:ASP453 2.7 25.9 1.0 OD1 A:ASP453 2.8 28.1 1.0 CG A:ASP387 2.9 26.7 1.0 CD2 A:HIS377 3.0 22.2 1.0 CE1 A:HIS377 3.0 24.2 1.0 OD2 A:ASP387 3.2 25.8 1.0 ZN A:ZN813 3.3 25.1 1.0 OE2 A:GLU425 3.7 23.8 1.0 OE1 A:GLU424 3.7 23.3 1.0 C7 A:JX5817 4.0 25.5 1.0 CD A:GLU424 4.1 23.5 1.0 ND1 A:HIS377 4.1 23.2 1.0 CG A:HIS377 4.1 22.8 1.0 CB A:ASP453 4.2 23.3 1.0 N3 A:JX5817 4.2 24.8 1.0 OE2 A:GLU424 4.2 23.3 1.0 CB A:ASP387 4.2 25.9 1.0 CB A:PRO388 4.3 25.6 1.0 C8 A:JX5817 4.3 27.9 1.0 ND2 A:ASN519 4.3 22.8 1.0 CD A:GLU425 4.4 24.0 1.0 O3 A:JX5817 4.4 27.8 1.0 CA A:PRO388 4.5 25.8 1.0 O A:HOH1220 4.5 30.2 0.6 CA A:ASP387 4.6 27.5 1.0 N A:PRO388 4.6 26.0 1.0 C A:ASP387 4.6 25.4 1.0 OE1 A:GLU425 4.7 24.3 1.0 N4 A:JX5817 4.8 24.0 1.0 CG A:GLU424 5.0 22.3 1.0 OG A:SER454 5.0 26.4 1.0

C.Barinka, Z.Kutil. X-Ray Structure of Human Glutamate Carboxypeptidase II (Gcpii) in Complex with A Inhibitor KB1157 To Be Published.